Differential Processing of Nuclear Pore Complex Proteins by Rhinovirus 2A Proteases from Different Species and Serotypes

Watters, Kelly; Palmenberg, Ann C.

doi:10.1128/jvi.00718-11

Cited by 73 publications

(94 citation statements)

References 44 publications

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“…Phosphorylation reactions. HeLa or BHK-21 cytosol from uninfected cells was prepared via Dounce homogenization (28). Rabbit reticulocyte lysates were commercial (Promega).…”

Section: Methodsmentioning

confidence: 99%

Encephalomyocarditis Virus Leader Is Phosphorylated by CK2 and Syk as a Requirement for Subsequent Phosphorylation of Cellular Nucleoporins

Basta

Bacot‐Davis

Ciomperlik

et al. 2014

J Virol

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“…Phosphorylation reactions. HeLa or BHK-21 cytosol from uninfected cells was prepared via Dounce homogenization (28). Rabbit reticulocyte lysates were commercial (Promega).…”

Section: Methodsmentioning

confidence: 99%

Encephalomyocarditis Virus Leader Is Phosphorylated by CK2 and Syk as a Requirement for Subsequent Phosphorylation of Cellular Nucleoporins

Basta

Bacot‐Davis

Ciomperlik

et al. 2014

J Virol

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“…This is noticed at the level of transcription, mRNA processing, nucleocytoplasmic transport, translation, or RNA granules composition. Among other proteins, proteolysis affects splicing factors, RNAprocessing proteins, RNA helicases, nuclear pore factors, stress granules assembly factors or antiviral response proteins (Almstead and Sarnow, 2007;Barral et al, 2009;Castello et al, 2009;Chen et al, 2013;Lawrence et al, 2012;Mukherjee et al, 2011;Park et al, 2010;Pineiro et al, 2012;Rozovics et al, 2012;Shiroki et al, 1999;Watters and Palmenberg, 2011;Weng et al, 2009;White et al, 2007).…”

Section: Picornavirus-induced Modification Of Host Factorsmentioning

confidence: 99%

Picornavirus IRES elements: RNA structure and host protein interactions

et al. 2015

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“…Specific Nups are cleaved during poliovirus or human rhinovirus infection, which results in the disruption of certain import/export pathways (15)(16)(17)(18)(19)(20). More recent work has demonstrated that poliovirus and human rhinovirus 2A proteinases can directly cleave specific Nups (17,18,20,21). Interestingly, human rhinovirus 2A proteinases from different species and serotypes show differential processing of nuclear pore complex proteins (20).…”

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confidence: 99%

“…Expression of poliovirus 2A proteinase in uninfected cells causes the cytoplasmic relocalization of some host nuclear factors, initially suggesting that 2A may be responsible for the degradation of nuclear pore complex proteins (or Nups) during infection (14). Specific Nups are cleaved during poliovirus or human rhinovirus infection, which results in the disruption of certain import/export pathways (15)(16)(17)(18)(19)(20). More recent work has demonstrated that poliovirus and human rhinovirus 2A proteinases can directly cleave specific Nups (17,18,20,21).…”

mentioning

confidence: 99%

“…More recent work has demonstrated that poliovirus and human rhinovirus 2A proteinases can directly cleave specific Nups (17,18,20,21). Interestingly, human rhinovirus 2A proteinases from different species and serotypes show differential processing of nuclear pore complex proteins (20).Viral protein 3CD is a precursor polypeptide containing the amino acid sequences of the 3C proteinase and the RNA-dependent RNA polymerase 3D. A major role of 3CD proteinase for enteroviruses and human rhinoviruses is the proteolytic processing of viral capsid precursors as well as the precursors leading to the production of mature nonstructural proteins (22,23).…”

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confidence: 99%

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Viral Proteinase Requirements for the Nucleocytoplasmic Relocalization of Cellular Splicing Factor SRp20 during Picornavirus Infections

Fitzgerald

Chase

Cathcart

et al. 2013

J Virol

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Infection of mammalian cells by picornaviruses results in the nucleocytoplasmic redistribution of certain host cell proteins. These viruses interfere with import-export pathways, allowing for the cytoplasmic accumulation of nuclear proteins that are then available to function in viral processes. We recently described the cytoplasmic relocalization of cellular splicing factor SRp20 during poliovirus infection. SRp20 is an important internal ribosome entry site (IRES) trans-acting factor (ITAF) for poliovirus IRES-mediated translation; however, it is not known whether other picornaviruses utilize SRp20 as an ITAF and direct its cytoplasmic relocalization. Also, the mechanism by which poliovirus directs the accumulation of SRp20 in the cytoplasm of the infected cell is currently unknown. Work described in this report demonstrated that infection by another picornavirus (coxsackievirus B3) causes SRp20 to relocalize from the nucleus to the cytoplasm of HeLa cells, similar to poliovirus infection; however, SRp20 is relocalized to a somewhat lesser extent in the cytoplasm of HeLa cells during infection by yet another picornavirus (human rhinovirus 16). We show that expression of poliovirus 2A proteinase is sufficient to cause the nucleocytoplasmic redistribution of SRp20. Following expression of poliovirus 2A proteinase in HeLa cells, we detect cleavage of specific nuclear pore proteins known to be cleaved during poliovirus infection. We also find that expression of human rhinovirus 16 2A proteinase alone can cause efficient cytoplasmic relocalization of SRp20, despite the lower levels of SRp20 relocalization observed during rhinovirus infection compared to poliovirus. Taken together, these results further define the mechanism of SRp20 cellular redistribution during picornavirus infections, and they provide additional insight into some of the differences observed between human rhinovirus and other enterovirus infections. Members of the Picornaviridae family of viruses cause a range of diseases in humans, including poliomyelitis, myocarditis, and the common cold. Picornaviruses are small single-stranded, positive-sense RNA viruses that include the enteroviruses poliovirus and coxsackievirus, as well as human rhinoviruses (HRVs). They contain a ϳ7.0-kb-to-8.5-kb genome that consists of a single open reading frame, which is translated to generate a polyprotein that is proteolytically processed by viral proteinases into structural and nonstructural proteins. Instead of a 7-methyl guanosine cap structure, picornaviruses contain a small viral protein, VPg, covalently linked to the 5= end of the RNA. This unique protein-RNA linkage serves as a primer for viral RNA synthesis. Viral translation occurs via a cap-independent mechanism and is driven by an internal ribosome entry site (IRES) located in the long, highly structured 5= noncoding region (5= NCR).In addition to proteolytic processing of the viral polyprotein, the viral proteinases 2A and 3C/3CD cleave several cellular proteins, including eukaryotic initiation factor 4G ...

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Differential Processing of Nuclear Pore Complex Proteins by Rhinovirus 2A Proteases from Different Species and Serotypes

Cited by 73 publications

References 44 publications

Encephalomyocarditis Virus Leader Is Phosphorylated by CK2 and Syk as a Requirement for Subsequent Phosphorylation of Cellular Nucleoporins

Encephalomyocarditis Virus Leader Is Phosphorylated by CK2 and Syk as a Requirement for Subsequent Phosphorylation of Cellular Nucleoporins

Picornavirus IRES elements: RNA structure and host protein interactions

Viral Proteinase Requirements for the Nucleocytoplasmic Relocalization of Cellular Splicing Factor SRp20 during Picornavirus Infections

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